A0A927BM48 · A0A927BM48_STRGL
- ProteinAdenosine deaminase
- Geneadd
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids384 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Catalytic activity
- 2'-deoxyadenosine + H2O + H+ = 2'-deoxyinosine + NH4+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 23 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 25 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 25 | substrate | ||||
Sequence: H | ||||||
Binding site | 27 | substrate | ||||
Sequence: D | ||||||
Binding site | 185 | substrate | ||||
Sequence: G | ||||||
Binding site | 212 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 215 | Proton donor | ||||
Sequence: E | ||||||
Site | 236 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 304 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | adenosine deaminase activity | |
Molecular Function | zinc ion binding | |
Biological Process | adenosine catabolic process | |
Biological Process | hypoxanthine salvage | |
Biological Process | inosine biosynthetic process | |
Biological Process | nucleotide metabolic process | |
Biological Process | purine ribonucleoside monophosphate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenosine deaminase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A927BM48
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-358 | Adenosine deaminase | ||||
Sequence: PKVLLHDHLDGGLRPGTVVELARAQGYDSLPETEPDKLGVWFREAADSGSLPRYLETFAHTCAVMQTREALFRVAAECAEDLAEDGVVYAEIRYAPEQHLEGGLTLEEVVEAVNEGFREGERVARANGHRIRVGALLTAMRHAARALEIAELANSYRDQGVVGFDIAGAEAGFPPTRHLDAFEYLKRENNHFTIHAGEAFGLPSIWQALQWCGADRLGHGVRIIDDIEVADDGSVTLGRLASYVRDKRIPLEMCPTSNLQTGAATSYAEHPIGLLRKLHFRITVNTDNRLMSGTSMSQEFERLTETFGYTLDDMQWFTVNAMKSAFIPFDERLAMINDVVK |
Sequence similarities
Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length384
- Mass (Da)42,482
- Last updated2023-02-22 v1
- ChecksumDDCF52DDC4388ECA